7B51

Crystal structure of human CRM1 covalently modified by 2-mercaptoethanol at Cys528

7B51 の概要

• エントリーDOI: 10.2210/pdb7b51/pdb
• 分子名称: GTP-binding nuclear protein Ran, Exportin-1, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: exportin, inhibition, nuclear protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 143374.38

構造登録者

Shaikhqasem, A.,Ficner, R. (登録日: 2020-12-03, 公開日: 2021-03-10, 最終更新日: 2024-01-31)

主引用文献

Shaikhqasem, A.,Schmitt, K.,Valerius, O.,Ficner, R.
Crystal structure of human CRM1, covalently modified by 2-mercaptoethanol on Cys528, in complex with RanGTP.
Acta Crystallogr.,Sect.F, 77:70-78, 2021

PubMed Abstract: CRM1 is a nuclear export receptor that has been intensively targeted over the last decade for the development of antitumor and antiviral drugs. Structural analysis of several inhibitor compounds bound to CRM1 revealed that their mechanism of action relies on the covalent modification of a critical cysteine residue (Cys528 in the human receptor) located in the nuclear export signal-binding cleft. This study presents the crystal structure of human CRM1, covalently modified by 2-mercaptoethanol on Cys528, in complex with RanGTP at 2.58 Å resolution. The results demonstrate that buffer components can interfere with the characterization of cysteine-dependent inhibitor compounds.

PubMed: 33682791
DOI: 10.1107/S2053230X2100203X

実験手法

X-RAY DIFFRACTION (2.58 Å)